Download full-text PDF |
Source |
---|
Genes Immun
January 2025
Department of Medicine, Medical University of South Carolina, Charleston, SC, USA.
Immunoglobulin GM (γ marker) and KM (κ marker) allotypes-encoded by immunoglobulin heavy chain G (IGHG) and immunoglobulin κ constant (IGKC) genes-have been shown to be associated with immune responsiveness to a variety of self and nonself antigens. The aim of the present investigation was to determine whether allelic variation at the GM and KM loci was associated with antibody responsiveness to poly-N-acetyl-D-glucosamine (PNAG), a broadly-conserved surface polysaccharide expressed by many microbial pathogens. In addition, we wished to determine whether Fcγ receptor 2 A (FCGR2A) genotypes, which have been shown to be risk factors for some pathogens, also influenced antibody responses to PNAG.
View Article and Find Full Text PDFbioRxiv
December 2024
Department of Neurology and Department of Epidemiology and Biostatistics, University of California San Francisco, CA, 94158, USA.
Killer-cell immunoglobulin-like receptors (s) are essential components of the innate immune system found on the surfaces of natural killer (NK) cells. The s encoding genes are located on chromosome 19q13.4 and are genetically diverse across populations.
View Article and Find Full Text PDFbioRxiv
November 2024
Department of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Lebanon, NH 03756, USA.
Herpes simplex virus (HSV) encodes surface glycoproteins that are host defense evasion molecules, allowing the virus to escape immune clearance. In addition to their role in neuropathogenesis and cell-cell spread, glycoproteins E and I (gE/gI) form a viral Fc receptor (vFcR) for most subclasses and allotypes of human IgG and promote evasion of humoral immune responses. While monoclonal antibodies (mAbs) protect mice from neonatal HSV (nHSV) infections, the impact of the vFcR on mAb-mediated protection by binding to IgG is unknown.
View Article and Find Full Text PDFFront Immunol
November 2024
Department of Immunology, Center for Innate Immunity and Immune Disease, School of Medicine, University of Washington, Seattle, WA, United States.
Front Immunol
November 2024
Laboratory of Biochemistry, Department of Chemistry, National and Kapodistrian University of Athens, Athens, Greece.
Introduction: ER aminopeptidase 1 (ERAP1) is a polymorphic intracellular aminopeptidase with key roles in antigen presentation and adaptive immune responses. ERAP1 allotype 10 is highly protective toward developing some forms of autoimmunity and displays unusual functional properties, including very low activity versus some substrates.
Methods: To understand the molecular mechanisms that underlie the biology of allotype 10, we studied its enzymatic and biophysical properties focusing on its unique polymorphisms V349M and Q725R.
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!